Skip to main content

Table 2 Data collection and refinement statistics

From: Enzyme intermediates captured “on the fly” by mix-and-inject serial crystallography

  Reference 30 ms 100 ms 500 ms 2 s
(a) Shard-shaped crystals
 Hits 98,895 35,065 88,413 158,620 39,140
 Indexed images 73,170 24,397 79,328 134,583 32,201
 Resolution (Å) 2.45 2.75 2.15 2.20 2.30
 Space group P21 P21 P21 P21 P21
 Unit cell (Å,o)
 (a, b, c, and β)
79.0 97.2
110.6 108.7
78.7 96.8
112.6 109.7
79.2 96.5
113.7 109.9
78.8 96.3
113.5 110.0
78.2 95.6
112.3109.9
 Volume (Å3) 804,442 807,597 817,098 809,346 789,415
 BlaC/unit cell 8 8 8 8 8
 Completeness 100(100) 100(100) 100(100) 100(100) 100(100)
 Multiplicity 1221 (103.3) 526 (142.0) 895 (58.8) 1363 (81.3) 330 (59.0)
 SNR 8.9(2.4) 6.4(0.9) 7.1(1.0) 8.3(0.9) 5.4(1.1)
 Rsplit (%) 9.8(209.4) 14.2(121.1) 11.18(111.0) 9.7(126.3) 11.9(104.1)
 CC-half (%) 99.4(41.1) 98.6(34.5) 99.4(37.5) 99.6(31.0) 96.8(35.4)
Refinement
 Rcryst/Rfree (%) 19.2/24.4 19.3/25.0 20.9/23.9 21.9/25.0 23.5/26.6
*BCEF/E-CFO*a 0/0 91 (23b) 57/32 40/36c 58/25
*DCEF/E-CFO*a 0/0 89 (24b) 54/40 38/44 51/31
 Stacking no yes yes yes yes
 H2O 315 143 499 431 399
 Average B value (Å2) 48.2 51.7 42.3 37.3 36.2
 Protein amino acid residues in asym. unit 265 × 4 265 × 4 265 × 4 265 × 4 265 × 4
 Ligands 0 2 + 2 (stacking) 2 + 2 (stacking) 2 + 2 (stacking) 2 + 2 (stacking)
 RMSD bond lengths (Å) 0.008 0.010 0.008 0.008 0.008
 RMSD bond angles (degrees) 1.10 1.72 1.66 1.67 1.74
 PO4 4 2 2 2 2
(b) Needle-shaped crystals
 Hits 171,314 64,507 115,223 141,935 36,606
 Indexed images 111,466 34,590 87,580 87,058 23,278
 Resolution (Å) 1.8 1.9 1.8 1.9 2.05
 Space group P21 P21 P21 P21 P21
 Unit cell (Å,o)
 (a, b, c, and β)
39.6 41.6
69.3 104.8
39.5 41.6
69.3 104.8
39.6 41.6
69.3 104.9
39.6 41.7
69.5 104.9
39.6 41.7
69.5 104.9
 Volume (Å3) 110,375 110,096 110,323 110,908 110,908
 Completeness (%) 100(100) 100(100) 100(100) 100(100) 100(100)
 Multiplicity 985 (54.5) 330 (26.8) 831 (89.0) 806 (36.5) 238 (27.3)
 Signal-to-noise ratio 9.6(1.2) 5.8(0.8) 9.6(1.6) 8.6(0.9) 5.1(1.1)
 Rsplit (%) 6.6(97.0) 12.2(136.3) 6.6(72.5) 8.8(129.1) 14.0(105.9)
 CC* (%) 99.9(75.0) 99.9(76.1) 99.9(84.3) 99.9(68.1) 99.8(74.8)
 CC-half (%) 99.7(39.1) 99.4(40.4) 99.7(55.1) 99.7(30.2) 99.13(38.8)
Refinement
 Rcryst/Rfree (%) 21.5/24.5 20.7/26.2 23.0/26.7 21.7/26.4 20.0/25.0
 Nd na 9 9 6 5
 CEF/E-CFO*a 0/0 59/0 51/35 43/53 71/0
 Stacking no no no no no
 H2O 167 203 154 104 175
 Average B value (Å2) 34.7 16.9 10.5 15.7 18.3
 Protein amino acid residues in asym. unit 265 265 265 265 265
 Ligands 0 1 1 1 1
 RMSD bond lengths (Å) 0.008 0.007 0.007 0.003 0.008
 RMSD bond angles (degrees) 1.06 1.57 1.74 1.49 1.57
  1. *Bfor subunit B
  2. *Dfor subunit D
  3. aoccupancy of full-length, intact CEF to covalently bound, open E-CFO*, which has lost R. Numbers are rough estimates and should represent only trends (the error is on the order of 25%, see note b)
  4. bomit maps show only CEF in the active site. If E-CFO*‘s occupancy is refined at the same time, values around 24% are obtained. We consider this the error of our occupancy refinement
  5. cAddition of OH instead of the double bond ∆
  6. dIf N does not extrapolate to 100% occupancy, a fraction of reference structure is present. This is ignored in the refinement
  7. na not applicable
  8. RMSD root mean square deviation